You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Structure of Membrane-Bound α-Synuclein Studied by Site-Directed Spin Labeling
Christine C. Jao, Ani Der-Sarkissian, Jeannie Chen, Ralf Langen and Harry B. Gray
Proceedings of the National Academy of Sciences of the United States of America
Vol. 101, No. 22 (Jun. 1, 2004), pp. 8331-8336
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3372187
Page Count: 6
You can always find the topics here!Topics: Proteins, Periodicity, Lipids, Wheels, Biochemistry, Unilamellar liposomes, Neuroscience, Phospholipids, Spectral methods, Line spectra
Were these topics helpful?See somethings inaccurate? Let us know!
Select the topics that are inaccurate.
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Many of the proposed physiological functions of α-synuclein, a protein involved in the pathogenesis of Parkinson's disease, are related to its ability to interact with phospholipids. To better understand the conformational changes that occur upon membrane binding of monomeric α-synuclein, we performed EPR analysis of 47 singly labeled α-synuclein derivatives. We show that membrane interaction is mediated by major conformational changes within seven N-terminal 11-aa repeats, which reorganize from a highly dynamic structure into an elongated helical structure devoid of significant tertiary packing. Furthermore, we find that analogous positions from different repeats are in equivalent locations with respect to membrane proximity. These and other findings suggest a curved membrane-dependent α-helical structure, wherein each 11-aa repeat takes up three helical turns. Similar helical structures could also apply to apolipoproteins and other lipid-interacting proteins with related 11-aa repeats.
Proceedings of the National Academy of Sciences of the United States of America © 2004 National Academy of Sciences